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1.
Biochem Biophys Res Commun ; 734: 150591, 2024 Aug 28.
Article in English | MEDLINE | ID: mdl-39255745

ABSTRACT

Breast cancer is a prominent cause of death among women and is distinguished by a high occurrence of metastasis. From this perspective, apart from conventional therapies, several alternative approaches have been researched and explored in recent years, including the utilization of nano-albumin and statin medications like simvastatin. The objective of this study was to prepare albumin nanoparticles incorporating simvastatin by the self-assembly method and evaluate their impact on breast cancer metastasis and apoptosis. The data showed the prepared nanoparticles have a diameter of 185 ± 24nm and a drug loading capacity of 8.85 %. The findings exhibit improved release in a lysosomal-like environment and under acidic pH conditions. MTT data showed that nanoparticles do not exhibit a dose-dependent effect on cells. Additionally, the results from MTT, flow cytometry, and qPCR analyses demonstrated that nanoparticles have a greater inhibitory and lethal effect on MDA-MB-231 cells compared to normal simvastatin. And cause cells to accumulate in the G0/G1 phase, initiating apoptotic pathways by inhibiting cell cycle progression. Nanoparticles containing simvastatin can prevent cell invasion and migration in both monolayer and spheroid models, as compared to simvastatin alone, at microscopic levels and in gene expression. The obtained data clearly showed that, compared to simvastatin, nanoparticles containing simvastatin demonstrated significant efficacy in suppressing the growth, proliferation, invasion, and migration of cancer cells in monolayer (2D) and spheroid (3D) models.

2.
Small ; 20(6): e2306466, 2024 Feb.
Article in English | MEDLINE | ID: mdl-37775327

ABSTRACT

Proteins exhibit complex and diverse multi-dimensional structures, along with a wide range of functional groups capable of binding metal ions. By harnessing the unique characteristics of proteins, it is possible to enhance the synthesis of metal-organic frameworks (MOFs) and modify their morphology. Here, the utilization of biomineralized bovine serum albumin (BSA) protein as a template for synthesizing Mil-100 with superior microwave absorption (MA) properties is investigated. The multi-dimensional structure and abundant functional groups of biomineralized BSA protein make it an ideal candidate for guiding the synthesis of Mil-100 with intricate network structures. The BSA@Mil-100 synthesized using this method exhibits exceptional uniformity and monodispersity of nanocrystals. The findings suggest that the BSA protein template significantly influences the regulation of nanocrystal and microstructure formation of Mil-100, resulting in a highly uniform and monodisperse structure. Notably, the synthesized 2-BSA@Mil-100 demonstrates a high reflection loss value of -58 dB at 8.85 GHz, along with a maximum effective absorption bandwidth value of 6.79 GHz, spanning from 6.01 to 12.8 GHz. Overall, this study highlights the potential of utilizing BSA protein as a template for MOF synthesis, offering an effective strategy for the design and development of high-performance MA materials.

3.
J Mol Recognit ; 37(4): e3084, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38596890

ABSTRACT

The binding of drugs to plasma proteins determines its fate within the physiological system, hence profound understanding of its interaction within the bloodstream is important to understand its pharmacodynamics and pharmacokinetics and thereby its therapeutic potential. In this regard, our work delineates the mechanism of interaction of Selumetinib (SEL), a potent anti-cancer drug showing excellent effect against multiple solid tumors, with plasma protein bovine serum albumin (BSA), using methods such as absorption, steady-state fluorescence, time-resolved, fluorescence resonance energy transfer, Fourier transform infrared spectra (FTIR), circular dichroism (CD), synchronous and 3D-fluorescence, salt fluorescence, molecular docking and molecular dynamic simulations. The BSA fluorescence intensity was quenched with increasing concentration of SEL which indicates interactions of SEL with BSA. Stern-Volmer quenching analysis and lifetime studies indicate the involvement of dynamic quenching. However, some contributions from the static quenching mechanism could not be ruled out unambiguously. The association constant was found to be 5.34 × 105 M-1 and it has a single binding site. The Förster distance (r) indicated probable energy transmission between the BSA and SEL. The positive entropy changes and enthalpy change indicate that the main interacting forces are hydrophobic forces, also evidenced by the results of molecular modeling studies. Conformation change in protein framework was revealed from FTIR, synchronous and 3D fluorescence and CD studies. Competitive binding experiments as well as docking studies suggest that SEL attaches itself to site I (subdomain IIA) of BSA where warfarin binds. Molecular dynamic simulations indicate the stability of the SEL-BSA complex. The association energy between BSA and SEL is affected in the presence of different metals differently.


Subject(s)
Antineoplastic Agents , Benzimidazoles , Circular Dichroism , Molecular Docking Simulation , Molecular Dynamics Simulation , Protein Binding , Serum Albumin, Bovine , Serum Albumin, Bovine/chemistry , Serum Albumin, Bovine/metabolism , Animals , Cattle , Antineoplastic Agents/chemistry , Antineoplastic Agents/pharmacology , Benzimidazoles/chemistry , Benzimidazoles/pharmacology , Binding Sites , Spectroscopy, Fourier Transform Infrared , Fluorescence Resonance Energy Transfer , Thermodynamics , Spectrometry, Fluorescence
4.
Mol Hum Reprod ; 30(3)2024 Feb 29.
Article in English | MEDLINE | ID: mdl-38341666

ABSTRACT

To become fertile, mammalian sperm are required to undergo capacitation in the female tract or in vitro in defined media containing ions (e.g. HCO3 -, Ca2+, Na+, and Cl-), energy sources (e.g. glucose, pyruvate) and serum albumin (e.g. bovine serum albumin (BSA)). These different molecules initiate sequential and concomitant signaling pathways, leading to capacitation. Physiologically, capacitation induces changes in the sperm motility pattern (e.g. hyperactivation) and prepares sperm for the acrosomal reaction (AR), two events required for fertilization. Molecularly, HCO3 - activates the atypical adenylyl cyclase Adcy10 (aka sAC), increasing cAMP and downstream cAMP-dependent pathways. BSA, on the other hand, induces sperm cholesterol release as well as other signaling pathways. How these signaling events, occurring in different sperm compartments and with different kinetics, coordinate among themselves is not well established. Regarding the AR, recent work has proposed a role for glycogen synthase kinases (GSK3α and GSK3ß). GSK3α and GSK3ß are inactivated by phosphorylation of residues Ser21 and Ser9, respectively, in their N-terminal domain. Here, we present evidence that GSK3α (but not GSK3ß) is present in the anterior head and that it is regulated during capacitation. Interestingly, BSA and HCO3 - regulate GSK3α in opposite directions. While BSA induces a fast GSK3α Ser21 phosphorylation, HCO3 - and cAMP-dependent pathways dephosphorylate this residue. We also show that the HCO3--induced Ser21 dephosphorylation is mediated by hyperpolarization of the sperm plasma membrane potential (Em) and by intracellular pH alkalinization. Previous reports indicate that GSK3 kinases mediate the progesterone-induced AR. Here, we show that GSK3 inhibition also blocks the Ca2+ ionophore ionomycin-induced AR, suggesting a role for GSK3 kinases downstream of the increase in intracellular Ca2+ needed for this exocytotic event. Altogether, our data indicate a temporal and biphasic GSK3α regulation with opposite actions of BSA and HCO3 -. Our results also suggest that this regulation is needed to orchestrate the AR during sperm capacitation.


Subject(s)
Glycogen Synthase Kinase 3 , Serum Albumin, Bovine , Sperm Capacitation , Animals , Female , Male , Mice , Calcium/metabolism , Cyclic AMP/metabolism , Glycogen Synthase Kinase 3/genetics , Glycogen Synthase Kinase 3/metabolism , Glycogen Synthase Kinase 3 beta/metabolism , Mammals , Phosphorylation , Semen/metabolism , Serum Albumin, Bovine/pharmacology , Serum Albumin, Bovine/metabolism , Sperm Motility , Spermatozoa/metabolism
5.
Chemistry ; : e202402582, 2024 Sep 10.
Article in English | MEDLINE | ID: mdl-39253847

ABSTRACT

Nano bimetallic oxides as nanoproteases have the great advantages in the heterogeneous hydrolysis of proteins. Here, we report that bimetallic delafossite CuFeO2 submicron particles (CuFeO2 SMPs) display a high protease activity towards selective cleavage of peptide bond involving hydrophobic residue at 25 centidegree. CuFeO2 SMPs have excellent regeneration performance with high structural stability. The strong Lewis acidity of Fe(III) and the strong nucleophilicity of Cu(I) bound hydroxyl groups are both necessary for the high protease activity of CuFeO2 SMPs. Low-valent metal ion has a great advantage in that low-valent Cu(I) bound hydroxyl has strong nucleophilicity, resulting in promotion of protein hydrolysis via high-efficient bimetallic catalysis. This study provides evidence that the protease activity of CuFeO2 SMPs depends on metal ion-bound hydroxyls on their surface. Our findings highlight that the valence of metal ions in artificial protease and their surface hydroxyls are two important factors that determine their catalytic efficiency.

6.
Chemphyschem ; 25(2): e202300505, 2024 Jan 15.
Article in English | MEDLINE | ID: mdl-38009440

ABSTRACT

Proteins can alter their shape when interacting with a surface. This study explores how bovine serum albumin (BSA) modifies structurally when it adheres to a gold surface, depending on the protein concentration and pH. We verified that the gold surface induces significant structural modifications to the BSA molecule using circular dichroism, infrared spectroscopy, and atomic force microscopy. Specifically, adsorbed molecules displayed increased levels of disordered structures and ß-turns, with fewer α-helices than the native structure. MP-SPR spectroscopy demonstrated that the protein molecules preferred a planar orientation during adsorption. Molecular dynamics simulations revealed that the interaction between cysteines exposed to the outside of the molecule and the gold surface was vital, especially at pH=3.5. The macroscopic properties of the protein film observed by AFM and contact angles confirm the flexible nature of the protein itself. Notably, structural transformation is joined with the degree of hydration of protein layers.


Subject(s)
Gold , Serum Albumin, Bovine , Gold/chemistry , Serum Albumin, Bovine/chemistry , Surface Properties , Protein Structure, Secondary , Circular Dichroism , Adsorption
7.
Nanotechnology ; 35(46)2024 Aug 29.
Article in English | MEDLINE | ID: mdl-39116890

ABSTRACT

The translation of silver-based nanotechnology 'from bench to bedside' requires a deep understanding of the molecular aspects of its biological action, which remains controversial at low concentrations and non-spherical morphologies. Here, we present a hemocompatibility approach based on the effect of the distinctive electronic charge distribution in silver nanoparticles (nanosilver) on blood components. According to spectroscopic, volumetric, microscopic, dynamic light scattering measurements, pro-coagulant activity tests, and cellular inspection, we determine that at extremely low nanosilver concentrations (0.125-2.5µg ml-1), there is a relevant interaction effect on the serum albumin and red blood cells (RBCs). This explanation has its origin in the surface charge distribution of nanosilver particles and their electron-mediated energy transfer mechanism. Prism-shaped nanoparticles, with anisotropic charge distributions, act at the surface level, generating a compaction of the native protein molecule. In contrast, the spherical nanosilver particle, by exhibiting isotropic surface charge, generates a polar environment comparable to the solvent. Both morphologies induce aggregation at NPs/bovine serum albumin ≈ 0.044 molar ratio values without altering the coagulation cascade tests; however, the spherical-shaped nanosilver exerts a negative impact on RBCs. Overall, our results suggest that the electron distributions of nanosilver particles, even at extremely low concentrations, are a critical factor influencing the molecular structure of blood proteins' and RBCs' membranes. Isotropic forms of nanosilver should be considered with caution, as they are not always the least harmful.


Subject(s)
Erythrocytes , Metal Nanoparticles , Serum Albumin, Bovine , Silver , Silver/chemistry , Metal Nanoparticles/chemistry , Erythrocytes/metabolism , Erythrocytes/chemistry , Humans , Serum Albumin, Bovine/chemistry , Serum Albumin, Bovine/metabolism , Surface Properties , Animals , Cattle , Blood Coagulation/drug effects , Blood Proteins/metabolism , Blood Proteins/chemistry , Materials Testing
8.
Nanotechnology ; 35(18)2024 Feb 15.
Article in English | MEDLINE | ID: mdl-38295400

ABSTRACT

Albumin is a vital blood protein responsible for transporting metabolites and drugs throughout the body and serves as a potential biomarker for various medical conditions, including inflammatory, cardiovascular, and renal issues. This report details the fabrication of Ni-metal organic framework/SnS2nanocomposite modified nickel foam electrochemical sensor for highly sensitive and selective non enzymatic detection of albumin in simulated human blood serum samples. Ni-metal organic framework/SnS2nanocomposite was synthesized using solvothermal technique by combining Ni-metal-organic framework (MOF) with conductive SnS2leading to the formation of a highly porous material with reduced toxicity and excellent electrical conductivity. Detailed surface morphology and chemical bonding of the Ni-MOF/SnS2nanocomposite was studied using scanning electron microscopy, transmission electron microscopy, Fourier transform infra-red, and Raman analysis. The Ni-MOF/SnS2nanocomposite coated on Ni foam electrode demonstrated outstanding electrochemical performance, with a low limit of detection (0.44µM) and high sensitivity (1.3µA/pM/cm2) throughout a broad linear range (100 pM-10 mM). The remarkable sensor performance is achieved through the synthesis of a Ni-MOF/SnS2nanocomposite, enhancing electrocatalytic activity for efficient albumin redox reactions. The enhanced performance can be attributed due to the structural porosity of nickel foam and Ni-metal organic framework, which favours increased surface area for albumin interaction. The presence of SnS2shows stability in acidic and neutral solutions due to high surface to volume ratio which in turn improves sensitivity of the sensing material. The sensor exhibited commendable selectivity, maintaining its performance even when exposed to potential interfering substances like glucose, ascorbic acid, K+, Na+, uric acid, and urea. The sensor effectively demonstrates its accuracy in detecting albumin in real samples, showcasing substantial recovery percentages of 105.1%, 110.28%, and 91.16%.


Subject(s)
Metal-Organic Frameworks , Nanocomposites , Humans , Metal-Organic Frameworks/chemistry , Nickel/chemistry , Serum , Electrodes , Electrochemical Techniques
9.
Environ Sci Technol ; 58(19): 8542-8553, 2024 May 14.
Article in English | MEDLINE | ID: mdl-38682869

ABSTRACT

The adsorption of foulants on photocatalytic nanoparticles can suppress their reactivity in water treatment applications by scavenging reactive species at the photocatalyst surface, screening light, or competing for surface sites. These inhibitory effects are commonly modeled using the Langmuir-Hinshelwood model, assuming that adsorbed layer compositions follow Langmuirian (equilibrium) competitive adsorption. However, this assumption has not been evaluated in complex mixtures of foulants. This study evaluates the photoreactivity of titanium dioxide (TiO2) nanoparticles toward a target compound, phenol, in the presence of two classes of foulants ─ natural organic matter (NOM) and a protein, bovine serum albumin (BSA) ─ and mixtures of the two. Langmuir adsorption models predict that BSA should strongly influence the nanoparticle photoreactivity because of its higher adsorption affinity relative to phenol and NOM. However, model evaluation of the experimental phenol decay rates suggested that neither the phenol nor foulant surface coverages are governed by Langmuirian competitive adsorption. Rather, a reactivity model incorporating kinetic predictions of adsorbed layer compositions (favoring NOM adsorption) outperformed Langmuirian models in providing accurate, unbiased predictions of phenol degradation rates. This research emphasizes the importance of using first-principles models that account for adsorption kinetics when assumptions of equilibrium adsorption do not apply.


Subject(s)
Nanoparticles , Adsorption , Kinetics , Nanoparticles/chemistry , Serum Albumin, Bovine/chemistry , Titanium/chemistry
10.
J Fluoresc ; 2024 May 13.
Article in English | MEDLINE | ID: mdl-38739318

ABSTRACT

A thiourea functionalised fluorescent probe 1-phenyl-3-(pyridin-4-yl)thiourea was synthesized and utilised as a fluorescent turn-on chemosensor for the selective recognition of Hg2+ ion over competitive metal ions including Na+, Mn2+, Li+, Cr2+, Ni2+, Ca2+, Cd2+, Mg2+, K+, Co2+, Cu2+, Zn2+, Al3+ and Fe2+ ions based on the inter-molecular charge transfer (ICT). Intriguingly, the receptor demonstrated unique sensing capabilities for Hg2+ in DMSO: H2O (10:90, v/v). The addition of Hg2+ ions to the sensor resulted in a blue shift in the absorption intensity and also enhancement in fluorescence intensity at 435 nm. Fluorescence emission intensity increased linearly with Hg2+ concentration ranging from 0 to 80 µL. The detection limit and binding constant were determined as 0.134 × 10-6 M and 1.733 × 107 M-1, respectively. The sensing behavior of Hg2+ was further examined using DLS, SEM and FTIR. The probe could detect Hg2+ ions across a wide pH range. Furthermore, the receptor L demonstrated good sensing performance for Hg2+ in bovine serum albumin and actual water samples.

11.
J Sep Sci ; 47(2): e2300864, 2024 Jan.
Article in English | MEDLINE | ID: mdl-38286728

ABSTRACT

In this study, we developed physically adsorbed multi-layer coatings using poly-l-lysine or poly(diallyldimethylammonium chloride) and gold nanoparticles, which were functionalized with bovine serum albumin for the chiral separation in electrochromatography. The approach involves sequentially depositing positively charged polymers and negatively charged citrate-stabilized gold nanoparticles. By repeating this modification cycle, we created two- and four-layer coatings, which were sequentially functionalized with albumin forming three- and five-layer coatings that were finally applied for the separation of enantiomers of dl-tryptophan. The formed coatings exhibit stability across a pH range of 2-10 and feature a dense, uniform surface, as confirmed by scanning electron microscope images. The number of layers impacted nanoparticle deposition density, with five-layer coatings being denser than three-layer ones. Five-layer coatings enable baseline separation of dl-tryptophan enantiomers, whereas three-layer coatings require the presence of albumin in the background electrolyte for separation. Therefore, increasing the number of layers and gold nanoparticles density enhances albumin active center concentration on capillary walls, improving the separation of dl-tryptophan enantiomers. The five-layer coatings can be easily fabricated and possess good repeatability of analytes migration time.


Subject(s)
Capillary Electrochromatography , Metal Nanoparticles , Serum Albumin, Bovine/chemistry , Capillary Electrochromatography/methods , Gold/chemistry , Tryptophan , Polymers/chemistry , Metal Nanoparticles/chemistry , Stereoisomerism
12.
J Reprod Dev ; 70(2): 131-137, 2024 Apr 04.
Article in English | MEDLINE | ID: mdl-38432992

ABSTRACT

Cold transport of the cauda epididymides is a useful technique for shipping laboratory rat sperm. Cold transport of rat sperm avoids potential risks of microbiological infection, animal escape or death, and animal welfare issues. Previously, we reported that a cold-storage solution containing dimethyl sulfoxide and quercetin maintained the fertility of cold-stored rat sperm. However, cold-stored rat sperm exhibited a decreased fertilization rate after 24-h storage. To recover the fertility of cold-stored sperm, we focused on the effects of bovine serum albumin (BSA), a cholesterol acceptor that induces sperm capacitation. We sought to determine the optimal concentration of BSA in fertilization medium based on the fertility of cold-stored rat sperm. High concentrations of BSA (40 mg/ml) enhanced the fertilization rate of cold-stored rat sperm and maintained sperm fertility for 144 h. Embryos derived from cold-stored and BSA-treated sperm normally developed into pups after embryo transfer. In summary, high BSA concentrations enhanced the fertility of cold-stored rat sperm and prolonged the storage period to 144 h, thereby expanding the transportable region for genetically engineered rats.


Subject(s)
Fertilization in Vitro , Serum Albumin, Bovine , Animals , Rats , Male , Serum Albumin, Bovine/pharmacology , Fertilization in Vitro/methods , Semen , Spermatozoa , Sperm Capacitation
13.
Luminescence ; 39(1): e4538, 2024 Jan.
Article in English | MEDLINE | ID: mdl-37312628

ABSTRACT

We aimed to synthesize hydroxyethyl starch (HES) 200/0.5-loaded bovine serum albumin nanoparticles (HBNs) and investigate the compatibility and binding mechanism in simulated physiological environments. Here, to elucidate the morphology, biocompatibility, and formation mechanism of HBNs, techniques such as scanning electron microscopy, haemolysis test, fluorescence, and circular dichroism spectroscopy were applied. The thermodynamic parameters at body temperature (ΔS° = -26.7 J·mol-1 ·K-1 , ΔH° = -3.20 × 104 J·mol-1 , and ΔG = -2.35 × 104 J·mol-1 ) showed a 1:1 binding stoichiometry, which was formed by hydrogen bonds and van der Waals interactions. In addition, the conformational analysis showed that the microenvironment of fluorophores was altered with the adaptational protein secondary structural changes. Energy transfer occurred from the fluorophores to HES with a high possibility. All these results provided accurate and complete primary data for demonstrating the interaction mechanisms of HES with BSA, which helps to understand its pharmaceutical effects in blood.


Subject(s)
Nanoparticles , Serum Albumin, Bovine , Binding Sites , Circular Dichroism , Spectrometry, Fluorescence/methods , Serum Albumin, Bovine/chemistry , Protein Binding , Thermodynamics , Starch
14.
Phytother Res ; 38(6): 2669-2686, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38500263

ABSTRACT

In the context of treating spinal cord injury (SCI), the modulation of inflammatory responses, and the creation of a suitable region for tissue regeneration may present a promising approach. This study aimed to evaluate the effects of curcumin (Cur)-loaded bovine serum albumin nanoparticles (Cur-BSA NPs) cross-linked with an acellular spinal cord scaffold (ASCS) on the functional recovery in a rat model of SCI. We developed an ASCS using chemical and physical methods. Cur-BSA, and blank (B-BSA) NPs were fabricated and cross-linked with ASCS via EDC-NHS, resulting in the production of Cur-ASCS and B-ASCS. We assessed the properties of scaffolds and NPs as well as their cross-links. Finally, using a male rat hemisection model of SCI, we investigated the consequences of the resulting scaffolds. The inflammatory markers, neuroregeneration, and functional recovery were evaluated. Our results showed that Cur was efficiently entrapped at the rate of 42% ± 1.3 in the NPs. Compared to B-ASCS, Cur-ASCS showed greater effectiveness in the promotion of motor recovery. The implantation of both scaffolds could increase the migration of neural stem cells (Nestin- and GFAP-positive cells) following SCI with the superiority of Cur-ASCS. Cur-ASCS was successful to regulate the gene expression and protein levels of NLRP3, ASC, and Casp1in the spinal cord lesion. Our results indicate that using ASCS can lead to the entrance of cells into the scaffold and promote neurogenesis. However, Cur-ASCS had greater effects in terms of inflammation relief and enhanced neurogenesis.


Subject(s)
Curcumin , Inflammasomes , NLR Family, Pyrin Domain-Containing 3 Protein , Neurogenesis , Rats, Sprague-Dawley , Recovery of Function , Spinal Cord Injuries , Spinal Cord , Tissue Scaffolds , Animals , Spinal Cord Injuries/drug therapy , Spinal Cord Injuries/therapy , Curcumin/pharmacology , NLR Family, Pyrin Domain-Containing 3 Protein/metabolism , Rats , Neurogenesis/drug effects , Inflammasomes/metabolism , Inflammasomes/drug effects , Male , Recovery of Function/drug effects , Tissue Scaffolds/chemistry , Spinal Cord/drug effects , Spinal Cord/metabolism , Nanoparticles/chemistry , Delayed-Action Preparations/pharmacology , Disease Models, Animal , Serum Albumin, Bovine/chemistry
15.
Chem Biodivers ; 21(7): e202400634, 2024 Jul.
Article in English | MEDLINE | ID: mdl-38726746

ABSTRACT

Molybdenum disulfide nanoflowers (MoS2 NFs) were prepared by hydrothermal method. The prepared MoS2 NFs was characterized by scanning electron microscopy (SEM), transmission electron microscopy (TEM), X-ray diffraction (XRD), specific surface areas, Raman and X-ray photoelectron spectroscopy (XPS). The characterization results show that the flower-like spherical MoS2 is composed of many ultra-thin nanosheets with an average diameter of about 300-400 nm. MoS2 NFs also exhibits excellent UV-vis absorption and high fluorescence intensity. In order to explore the biological behavior of MoS2 NFs, the interaction between MoS2 NFs and bovine serum albumin (BSA) was studied by UV-Vis absorption, fluorescence, synchronous fluorescence spectra, and cyclic voltammetry. The results of absorption and fluorescence show that MoS2 NFs and BSA interact strongly through the formation of complexes in the ground state, and the static quenching is the main mechanism. The Stern-Volmer constant and the quenching constant was calculated about 3.79×107 L mol-1 and 3.79×1015 L mol-1 s-1, respectively. The synchronous fluorescence implied that MoS2 in the complex may mainly bind to tryptophan residues of BSA. The cyclic voltammograms indicated that the addition of BSA makes electron reduction of MoS2 NFs more difficult than the corresponding free state. The results show that hydrophobic forces play a major role in the binding interaction between BSA and MoS2 NFs.


Subject(s)
Disulfides , Molybdenum , Nanostructures , Serum Albumin, Bovine , Spectrometry, Fluorescence , Serum Albumin, Bovine/chemistry , Serum Albumin, Bovine/metabolism , Molybdenum/chemistry , Disulfides/chemistry , Animals , Cattle , Nanostructures/chemistry , Spectrophotometry, Ultraviolet , Particle Size , Photoelectron Spectroscopy , Surface Properties
16.
Environ Toxicol ; 2024 Jun 25.
Article in English | MEDLINE | ID: mdl-38923375

ABSTRACT

The interaction between particles and proteins is a key factor determining the toxicity responses of particles. Therefore, this study aimed to examine the interaction between the emerging pollutant polyethylene terephthalate micro/nanoplastics from water bottles with bovine serum albumin. The physicochemical characteristics of micro/nanoplastics were investigated using nuclear magnetic resonance, x-ray diffraction, Fourier transform infrared, dynamic light scattering, and x-ray energy dispersive spectroscopy after exposure to various concentrations and durations of protein. Furthermore, the impact of protein-treated micro/nanoplastics on biological activities was examined using the mitochondrial activity and membrane integrity of A549 cells and the activity and biofilm production of Staphylococcus aureus. The structural characteristics of micro/nanoplastics revealed an interaction with protein. For instance, the assignment of protein-related new proton signals (e.g., CH2, methylene protons of CH2O), changes in available protons s (e.g., CH and CH3), crystallinity, functional groups, elemental ratios, zeta potentials (-11.3 ± 1.3 to -12.4 ± 1.7 to 25.5 ± 2.3 mV), and particle size (395 ± 76 to 496 ± 60 to 866 ± 82 nm) of micro/nanoplastics were significantly observed after protein treatment. In addition, the loading (0.012-0.027 mM) and releasing (0.008-0.013 mM) of protein also showed similar responses with structural characteristics. Moreover, the cell-based responses were changed regarding the structural and surface characteristics of micro/nanoplastics and the loading efficiencies of protein. For example, insignificant mitochondrial activity (2%-10%) and significant membrane integrity (12%-28%) of A549 cells increased compared with control, and reductions in bacterial activity (5%-40%) in many cases and biofilm production specifically at low dose of all treatment stages (13%-46% reduction) were observed.

17.
Sensors (Basel) ; 24(11)2024 Jun 04.
Article in English | MEDLINE | ID: mdl-38894440

ABSTRACT

Quasi-bound state in the continuum (QBIC) can effectively enhance the interaction of terahertz (THz) wave with matter due to the tunable high-Q property, which has a strong potential application in the detection of low-concentration biological samples in the THz band. In this paper, a novel THz metamaterial sensor with a double-chain-separated resonant cavity structure based on QBIC is designed and fabricated. The process of excitation of the QBIC mode is verified and the structural parameters are optimized after considering the ohmic loss by simulations. The simulated refractive index sensitivity of the sensor is up to 544 GHz/RIU, much higher than those of recently reported THz metamaterial sensors. The sensitivity of the proposed metamaterial sensor is confirmed in an experiment by detecting low-concentration lithium citrate (LC) and bovine serum albumin (BSA) solutions. The limits of detection (LoDs) are obtained to be 0.0025 mg/mL (12 µM) for LC and 0.03125 mg/mL (0.47 µM) for BSA, respectively, both of which excel over most of the reported results in previous studies. These results indicate that the proposed THz metamaterial sensor has excellent sensing performances and can well be applied to the detection of low-concentration biological samples.


Subject(s)
Biosensing Techniques , Serum Albumin, Bovine , Serum Albumin, Bovine/chemistry , Biosensing Techniques/methods , Biosensing Techniques/instrumentation , Limit of Detection , Animals , Terahertz Radiation , Cattle , Terahertz Spectroscopy/methods , Refractometry , Lithium Compounds/chemistry , Citric Acid/chemistry
18.
Sensors (Basel) ; 24(3)2024 Jan 30.
Article in English | MEDLINE | ID: mdl-38339622

ABSTRACT

A novel conductive composite based on PEDOT:PSS, BSA, and Nafion for effective immobilization of acetic acid bacteria on graphite electrodes as part of biosensors and microbial fuel cells has been proposed. It is shown that individual components in the composite do not have a significant negative effect on the catalytic activity of microorganisms during prolonged contact. The values of heterogeneous electron transport constants in the presence of two types of water-soluble mediators were calculated. The use of the composite as part of a microbial biosensor resulted in an electrode operating for more than 140 days. Additional modification of carbon electrodes with nanomaterial allowed to increase the sensitivity to glucose from 1.48 to 2.81 µA × mM-1 × cm-2 without affecting the affinity of bacterial enzyme complexes to the substrate. Cells in the presented composite, as part of a microbial fuel cell based on electrodes from thermally expanded graphite, retained the ability to generate electricity for more than 120 days using glucose solution as well as vegetable extract solutions as carbon sources. The obtained data expand the understanding of the composition of possible matrices for the immobilization of Gluconobacter bacteria and may be useful in the development of biosensors and biofuel cells.


Subject(s)
Graphite , Polymers , Polymers/chemistry , Serum Albumin, Bovine , Carbon/chemistry , Bacteria , Glucose/chemistry
19.
Inflammopharmacology ; 32(4): 2505-2524, 2024 Aug.
Article in English | MEDLINE | ID: mdl-38702577

ABSTRACT

Inflammatory responses play a crucial role in the pathophysiology of spinal cord injury (SCI) and developing new approaches to establish an anti-inflammatory environment for the promotion of neuroregeneration holds promise as a potential approach. In this study, our aim was to investigate the potential of combining an acellular spinal cord scaffold (ASCS) with quercetin-loaded bovine serum albumin (Qu/BSA) nanoparticles (NPs) for the treatment of SCI. The ASCS was prepared using physical and chemical methods, while the Qu/BSA NPs were prepared through a desolvation technique. The NPs exhibited favorable characteristics, including a mean size of 203 nm, a zeta potential of -38, and an encapsulation efficiency of 96%. Microscopic evaluation confirmed the successful distribution of NPs on the walls of ASCS. Animal studies revealed that Qu/BSA NPs group exhibited a significant decrease in NLRP3, ASC, and Casp1 gene expression compared to the SCI group (p < 0.0001). The findings indicated a significant decrease in the NLRP3, ASC, and Casp1 protein level between the Qu/BSA/ASCS group and the SCI group (p < 0.0001). Moreover, treatment with ASCS containing either blank BSA (B/BSA) NPs or Qu/BSA NPs effectively promoted functional recovery via increasing the amount of nestin- and glial fibrillary acidic protein (GFAP)-positive cells in the site of injury. Notably, Qu/BSA/ASCS exhibited superior outcomes compared to B/BSA/ASCS. Overall, the combination of ASCS with the Qu delivery system presents a promising therapeutic approach for SCI by inhibiting inflammatory responses and promoting neuroregeneration, leading to the restoration of motor function in animals. This study demonstrates the potential of utilizing biomaterials and NPs to enhance the effectiveness of SCI treatment.


Subject(s)
Anti-Inflammatory Agents , Nanoparticles , Quercetin , Recovery of Function , Spinal Cord Injuries , Spinal Cord , Animals , Spinal Cord Injuries/drug therapy , Spinal Cord Injuries/therapy , Quercetin/pharmacology , Quercetin/administration & dosage , Rats , Nanoparticles/administration & dosage , Recovery of Function/drug effects , Anti-Inflammatory Agents/pharmacology , Anti-Inflammatory Agents/administration & dosage , Spinal Cord/drug effects , Spinal Cord/metabolism , Tissue Scaffolds , Rats, Sprague-Dawley , Serum Albumin, Bovine/administration & dosage , Male
20.
Molecules ; 29(16)2024 Aug 07.
Article in English | MEDLINE | ID: mdl-39202815

ABSTRACT

Sonosensitizers play a crucial role in the efficacy of sonodynamic antitumor therapy (SDT) and sonodynamic antimicrobial chemotherapy (SACT), highlighting the necessity for the development of new compounds with good sonodynamic activity. In this study, three novel 3-substituted ciprofloxacin derivatives (CIPD1, CIPD2, and CIPD3) were designed and synthesized. Their sonodynamic activities were evaluated by assessing the damage to bovine serum albumin (BSA) and Escherichia coli (E. coli). Furthermore, the potential mechanism underlying their sonodynamic damage activities was investigated by detecting reactive oxygen species (ROS) under ultrasound irradiation (US). The results demonstrated that all three derivatives exhibited enhanced sonodynamic damage to BSA and E. coli under US, with CIPD1 and CIPD2 showing superior effectiveness compared to CIP. Both the concentrations of derivatives and the duration of ultrasound irradiation were found to significantly impact their sonodynamic effects. All three CIP derivates could be activated to produce ROS following ultrasound irradiation, primarily consisting of 1O2 and ·OH. The levels of ROS production were positively correlated with their sonodynamic activities, potentially explaining the mechanism underlying their sonodynamic damage activities.


Subject(s)
Ciprofloxacin , Escherichia coli , Reactive Oxygen Species , Serum Albumin, Bovine , Ciprofloxacin/pharmacology , Ciprofloxacin/chemistry , Reactive Oxygen Species/metabolism , Escherichia coli/drug effects , Serum Albumin, Bovine/chemistry , Ultrasonic Waves , Animals , Anti-Bacterial Agents/pharmacology , Anti-Bacterial Agents/chemistry , Anti-Bacterial Agents/chemical synthesis
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